BMRB Entry 19758

Name: 1H, 15N and 13C resonance assignments of the two TPR domains of the human RPAP3 protein
Published: 2019-08-13

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PDB ID: 6fd7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19758
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 1H, 15N and 13C resonance assignments of the two TPR domains of the human RPAP3 protein PubMed: 24668569

Deposition date: 2014-01-30 Original release date: 2019-08-13

Authors: Chagot, Marie-Eve; Jacquemin, Cl mence; Charpentier, Bruno; Manival, Xavier; Quinternet, Marc

Citation: Chagot, Marie-Eve; Jacquemin, Clemence; Branlant, Christiane; Charpentier, Bruno; Manival, Xavier; Quinternet, Marc. "(1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein." Biomol. NMR Assignments 9, 99-102 (2014).

Assembly members:
rpap3(133-255), polymer, 127 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
rpap3(133-255): GPHMALVLKEKGNKYFKQGK YDEAIDCYTKGMDADPYNPV LPTNRASAYFRLKKFAVAES DCNLAVALNRSYTKAYSRRG AARFALQKLEEAKKDYERVL ELEPNNFEATNELRKISQAL ASKENSY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	537
15N chemical shifts	132
1H chemical shifts	880

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TPR1	1

Entities:

Entity 1, TPR1 127 residues - Formula weight is not available

1

GLY

PRO

HIS

MET

ALA

LEU

VAL

LEU

LYS

GLU

2

LYS

GLY

ASN

LYS

TYR

PHE

LYS

GLN

GLY

LYS

3

TYR

ASP

GLU

ALA

ILE

ASP

CYS

TYR

THR

LYS

4

GLY

MET

ASP

ALA

ASP

PRO

TYR

ASN

PRO

VAL

5

LEU

PRO

THR

ASN

ARG

ALA

SER

ALA

TYR

PHE

6

ARG

LEU

LYS

PHE

ALA

VAL

ALA

GLU

SER

7

ASP

CYS

ASN

LEU

ALA

VAL

ALA

LEU

ASN

ARG

8

SER

TYR

THR

LYS

ALA

TYR

SER

ARG

GLY

9

ALA

ARG

PHE

ALA

LEU

GLN

LYS

LEU

GLU

10

GLU

ALA

LYS

ASP

TYR

GLU

ARG

VAL

LEU

11

GLU

LEU

GLU

PRO

ASN

PHE

GLU

ALA

THR

12

ASN

GLU

LEU

ARG

LYS

ILE

SER

GLN

ALA

LEU

13

ALA

SER

LYS

GLU

ASN

SER

TYR

Samples:

sample_1: rpap3(133-255), [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride 150 mM; DTT, [U-99% 2H], 10 mM; H2O 95%; D2O, [U-100% 2H], 5%

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts